2vtf: Difference between revisions

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{{Seed}}
[[Image:2vtf.png|left|200px]]
[[Image:2vtf.png|left|200px]]


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==About this Structure==
==About this Structure==
2VTF is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Arthrobacter_protophormiae Arthrobacter protophormiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VTF OCA].  
[[2vtf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arthrobacter_protophormiae Arthrobacter protophormiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VTF OCA].  


==Reference==
==Reference==
<ref group="xtra">PMID:19327363</ref><references group="xtra"/>
<ref group="xtra">PMID:019327363</ref><references group="xtra"/>
[[Category: Arthrobacter protophormiae]]
[[Category: Arthrobacter protophormiae]]
[[Category: Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase]]
[[Category: Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase]]
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[[Category: Glycosidase]]
[[Category: Glycosidase]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May  6 10:05:15 2009''

Revision as of 05:14, 24 August 2011

File:2vtf.png

Template:STRUCTURE 2vtf

X-RAY CRYSTAL STRUCTURE OF THE ENDO-BETA-N-ACETYLGLUCOSAMINIDASE FROM ARTHROBACTER PROTOPHORMIAE E173Q MUTANT REVEALS A TIM BARREL CATALYTIC DOMAIN AND TWO ANCILLARY DOMAINS

Template:ABSTRACT PUBMED 19327363

About this Structure

2vtf is a 2 chain structure with sequence from Arthrobacter protophormiae. Full crystallographic information is available from OCA.

Reference

  1. Ling Z, Suits MD, Bingham RJ, Bruce NC, Davies GJ, Fairbanks AJ, Moir JW, Taylor EJ. The X-ray crystal structure of an Arthrobacter protophormiae endo-beta-N-acetylglucosaminidase reveals a (beta/alpha)(8) catalytic domain, two ancillary domains and active site residues key for transglycosylation activity. J Mol Biol. 2009 May 29;389(1):1-9. Epub 2009 Mar 24. PMID:19327363 doi:10.1016/j.jmb.2009.03.050

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